BMRB Entry 16378

Name: Chemical shift assignment of GtR34C from Geobacillus thermodenitrificans. North East Structural Genomics Consortium Target GtR34C
Published: 2009-07-07

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PDB ID: 2kl1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16378
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Chemical shift assignment of GtR34C from Geobacillus thermodenitrificans. North East Structural Genomics Consortium Target GtR34C

Deposition date:

2009-06-29

Original release date:

2009-07-07

Authors:

Lee, Hsiau-Wei; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, GVT; Evertt, John; Montelione, Gaetano; Prestegard, James

Citation:

Citation: Lee, Hsiau-Wei; Montelione, Gaetano; Prestegard, James. "Solution Structure of GtR34C" .

Assembly members:

Assembly members:
GtR34C, polymer, 174 residues, 19278.225 Da.

Natural source:

Natural source: Common Name: Geobacillus thermodenitrificans Taxonomy ID: 33940 Superkingdom: Bacteria Kingdom: not available Genus/species: Geobacillus thermodenitrificans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Geobacillus thermodenitrificans Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GtR34C: MNEAKGVYVMSVLPNMPAAG RLEAGDRIAAIDGQPINTSE QIVSYVREKQAGDRVRVTFI RDRKQHEAELVLKPFPHHPN QIGLGVTMNEAKGVYVMSVL PNMPAAGRLEAGDRIAAIDG QPINTSEQIVSYVREKQAGD RVRVTFIRDRKQHEAELVLK PFPHHPNQIGLGVT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- PEG_RDC
- GEL_RDC

Data type	Count
13C chemical shifts	324
15N chemical shifts	76
1H chemical shifts	523
residual dipolar couplings	125

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GtR34C	1

Entities:

Entity 1, GtR34C 174 residues - 19278.225 Da.

LEHHHHHH are at the C-terminal as part of Hig-Tag. It is not included in the coordinate file.

1

MET

ASN

GLU

ALA

LYS

GLY

VAL

TYR

VAL

MET

2

SER

VAL

LEU

PRO

ASN

MET

PRO

ALA

GLY

3

ARG

LEU

GLU

ALA

GLY

ASP

ARG

ILE

ALA

4

ILE

ASP

GLY

GLN

PRO

ILE

ASN

THR

SER

GLU

5

GLN

ILE

VAL

SER

TYR

VAL

ARG

GLU

LYS

GLN

6

ALA

GLY

ASP

ARG

VAL

ARG

VAL

THR

PHE

ILE

7

ARG

ASP

ARG

LYS

GLN

HIS

GLU

ALA

GLU

LEU

8

VAL

LEU

LYS

PRO

PHE

PRO

HIS

PRO

ASN

9

GLN

ILE

GLY

LEU

GLY

VAL

THR

MET

ASN

GLU

10

ALA

LYS

GLY

VAL

TYR

VAL

MET

SER

VAL

LEU

11

PRO

ASN

MET

PRO

ALA

GLY

ARG

LEU

GLU

12

ALA

GLY

ASP

ARG

ILE

ALA

ILE

ASP

GLY

13

GLN

PRO

ILE

ASN

THR

SER

GLU

GLN

ILE

VAL

14

SER

TYR

VAL

ARG

GLU

LYS

GLN

ALA

GLY

ASP

15

ARG

VAL

ARG

VAL

THR

PHE

ILE

ARG

ASP

ARG

16

LYS

GLN

HIS

GLU

ALA

GLU

LEU

VAL

LEU

LYS

17

PRO

PHE

PRO

HIS

PRO

ASN

GLN

ILE

GLY

18

LEU

GLY

VAL

THR

Samples:

sample_1: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; H2O 95%; D2O 5%

PEG: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; C12E5 PEG/Hexanol 4.2%; H2O 95%; D2O 5%

GEL: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; Negatively Charged Compressed Polyacrylamide Gel 7%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: ambient atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 15N HSQCTROSY	PEG	isotropic	sample_conditions_1
2D 15N HSQCTROSY	GEL	isotropic	sample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PSVS, Bhattacharya and Montelione - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

Varian INOVA 600 MHz